Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2396434812  90 LKPDIAAPGVDILAAYTPANKD----QGDSYEFLSGTSMACPHVSGIVALIKSLHPNWSPAAIRSALVTTAS 157
Cdd:cd04852   236 LKPDIAAPGVDILAAWTPEGADpgdaRGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307

Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2396434812  90 LKPDIAAPGVDILAAYTPANKD----QGDSYEFLSGTSMACPHVSGIVALIKSLHPNWSPAAIRSALVTTAS 157
Cdd:cd04852   236 LKPDIAAPGVDILAAWTPEGADpgdaRGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307

Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  74 LASFSSRGPSSITPevLKPDIAAPGVDILAAYTPANKDQGDS------YEFLSGTSMACPHVSGIVALIKSLHPNWSPAA 147
Cdd:pfam00082 186 LASFSSYGPTLDGR--LKPDIVAPGGNITGGNISSTLLTTTSdppnqgYDSMSGTSMATPHVAGAAALLKQAYPNLTPET 263

                          90
                  ....*....|....*.
gi 2396434812 148 IRSALVTTASQTGTDG 163
Cdd:pfam00082 264 LKALLVNTATDLGDAG 279

PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2396434812   8 VFQAGGVGLIYAQFHTDGIEL---CEWIPCVKVDYEVGTQILSYIRQARSPTAKL 59
Cdd:cd02120    72 VKAAGGAGMILANDPTDGLDVvadAHVLPAVHVDYEDGTAILSYINSTSNPTATI 126

subtilisin-like protease; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2396434812  94 IAAPGVDILAAyTPANkdqgdSYEFLSGTSMACPHVSGIVALIKSLHPNWSPAAI----RSALVTTAS 157
Cdd:PTZ00262  534 LAAPGTNIYST-FPKN-----SYRKLNGTSMAAPHVAAIASLILSINPSLSYEEVirilKESIVQLPS 595

Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2396434812  90 LKPDIAAPGVDILAAYTPANKD----QGDSYEFLSGTSMACPHVSGIVALIKSLHPNWSPAAIRSALVTTAS 157
Cdd:cd04852   236 LKPDIAAPGVDILAAWTPEGADpgdaRGEDFAFISGTSMASPHVAGVAALLKSAHPDWSPAAIKSALMTTAY 307

Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  73 RLASFSSRGPssitpevlKPDIAAPGVDILAAYTpankdqGDSYEFLSGTSMACPHVSGIVALIKSLHPNWSPAAIRSAL 152
Cdd:COG1404   272 QLASFSNYGP--------KVDVAAPGVDILSTYP------GGGYATLSGTSMAAPHVAGAAALLLSANPDLTPAQVRAIL 337

                          90
                  ....*....|.
gi 2396434812 153 VTTASQTGTDG 163
Cdd:COG1404   338 LNTATPLGAPG 348

Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  74 LASFSSRGPssitpEVlkpDIAAPGVDILAAYTpankdqGDSYEFLSGTSMACPHVSGIVALIKSLHPNWSPAAIRSALV 153
Cdd:cd07477   162 RASFSSTGP-----EV---ELAAPGVDILSTYP------NNDYAYLSGTSMATPHVAGVAALVWSKRPELTNAQVRQALN 227

                  ..
gi 2396434812 154 TT 155
Cdd:cd07477   228 KT 229

Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  73 RLASFSSRGPssiTPE-VLKPDIAAPGVDILAAYTPA---NKDQGDSYEFLSGTSMACPHVSGIVALIKSLHPNWSPAAI 148
Cdd:cd07487   179 GISYFSSRGP---TGDgRIKPDVVAPGENIVSCRSPGgnpGAGVGSGYFEMSGTSMATPHVSGAIALLLQANPILTPDEV 255

                  ....*...
gi 2396434812 149 RSALVTTA 156
Cdd:cd07487   256 KCILRDTA 263

Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  75 ASFSSRGPssiTPE-VLKPDIAAPGVDILAAYTpankDQGDSYEFLSGTSMACPHVSGIVALIKSL-HPNWSPAAIRSAL 152
Cdd:cd07489   189 SYFSSWGP---TNElYLKPDVAAPGGNILSTYP----LAGGGYAVLSGTSMATPYVAGAAALLIQArHGKLSPAELRDLL 261

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2396434812 153 VTTASQT-GTDGmkifeEGSTRKEADPFDMGGGHVNPEKAAYpglvYDTT 201
Cdd:cd07489   262 ASTAKPLpWSDG-----TSALPDLAPVAQQGAGLVNAYKALY----ATTT 302

Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  73 RLASFSSRGPssitpevlKPDIAAPGVDILAAYTPANkdqgDSYEFLSGTSMACPHVSGIVALIKSLHPNWSPAAIRSAL 152
Cdd:cd00306   171 PASPSSNGGA--------GVDIAAPGGDILSSPTTGG----GGYATLSGTSMAAPIVAGVAALLLSANPDLTPAQVKAAL 238

                  ...
gi 2396434812 153 VTT 155
Cdd:cd00306   239 LST 241

Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  73 RLASFSSRGPssitpEVlkpDIAAPGVDILAaYTPANkdqgdSYEFLSGTSMACPHVSGIVALIKSLHPnWSPAAIRSAL 152
Cdd:cd07484   188 KRASFSNYGK-----WV---DVSAPGGGILS-TTPDG-----DYAYMSGTSMATPHVAGVAALLYSQGP-LSASEVRDAL 252

                  ....*...
gi 2396434812 153 VTTASQTG 160
Cdd:cd07484   253 KKTADDIG 260

Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores. Analysis of an enzyme fraction of GSP showed that it was composed of a gene cluster containing the processed forms of products of cspA, cspB, and cspC which are positioned in a tandem array just upstream of the 5' end of sleC. The amino acid sequences deduced from the nucleotide sequences of the csp genes showed significant similarity and showed a high degree of homology with those of the catalytic domain and the oxyanion binding region of subtilisin-like serine proteases. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  74 LASFSSRGPssITPEVLKPDIAAPGVDILAAYtpankdQGDSYEFLSGTSMACPHVSGIVALI------KSLHPNWSPAA 147
Cdd:cd07478   359 IAIFSGRGP--TRDGRIKPDIAAPGVNILTAS------PGGGYTTRSGTSVAAAIVAGACALLlqwgivRGNDPYLYGEK 430

                          90
                  ....*....|....*
gi 2396434812 148 IRSALVTTASQTGTD 162
Cdd:cd07478   431 IKTYLIRGARRRPGD 445

Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  73 RLASFSSRGPSSitpevlkpDIAAPGVDILaayTPANKDQ------------GDSYEFLSGTSMACPHVSGIVALIKSLH 140
Cdd:cd07496   202 QRASYSNYGPAV--------DVSAPGGDCA---SDVNGDGypdsntgttspgGSTYGFLQGTSMAAPHVAGVAALMKSVN 270

                          90
                  ....*....|....*
gi 2396434812 141 PNWSPAAIRSALVTT 155
Cdd:cd07496   271 PSLTPAQIESLLQST 285

Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  73 RLASFSSRGPSSITpevlKPDIAAPGVDILAAYTpankdqGDSYEFLSGTSMACPHVSGIVALI-------KSLHPNWSP 145
Cdd:cd07480   198 RTGNFSAVANFSNG----EVDIAAPGVDIVSAAP------GGGYRSMSGTSMATPHVAGVAALWaealpkaGGRALAALL 267

                          90
                  ....*....|....*..
gi 2396434812 146 AAIRSALVTTASQTGTD 162
Cdd:cd07480   268 QARLTAARTTQFAPGLD 284

Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include endopeptidases and exopeptidases. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  71 SPRLASFSSRGPSSI---TPEVL-KPDIAAP-GVDILAAYTpankdqGDSYEFLSGTSMACPHVSGIVALIKSLHPNWSP 145
Cdd:cd05562   166 PAPGGTPSSFDPVGIrlpTPEVRqKPDVTAPdGVNGTVDGD------GDGPPNFFGTSAAAPHAAGVAALVLSANPGLTP 239

                          90
                  ....*....|....*...
gi 2396434812 146 AAIRSALVTTASQTGTDG 163
Cdd:cd05562   240 ADIRDALRSTALDMGEPG 257

Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  73 RLASFSSRGPSSitpevlkpDIAAPGVDI---LAAYTPANKDQGDSYEFLSGTSMACPHVSGIVALIKSLHPNWSPAAIR 149
Cdd:cd07498   165 ARASYSNYGNYV--------DLVAPGVGIwttGTGRGSAGDYPGGGYGSFSGTSFASPVAAGVAALILSANPNLTPAEVE 236

                  ....*.
gi 2396434812 150 SALVTT 155
Cdd:cd07498   237 DILTST 242

Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine proteases belong to Peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2396434812  94 IAAPGVDILAAYTpankDQGDSYEFLSGTSMACPHVSGIVALIKSLHPNWSPAAIRSALVTTA 156
Cdd:cd04848   208 LAAPGENIYSTDP----DGGNGYGRVSGTSFAAPHVSGAAALLAQKFPWLTADQVRQTLLTTA 266

PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2396434812   8 VFQAGGVGLIYAQFHTDGIEL---CEWIPCVKVDYEVGTQILSYIRQARSPTAKL 59
Cdd:cd02120    72 VKAAGGAGMILANDPTDGLDVvadAHVLPAVHVDYEDGTAILSYINSTSNPTATI 126

bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2396434812   78 SSRGPSSItpEVLKPDIAAPGVDILAAYtPANKdqgdsYEFLSGTSMACPHVSGIVAL 135
Cdd:NF040809   994 SSRGPTIR--NIQKPDIVAPGVNIIAPY-PGNT-----YATITGTSAAAAHVSGVAAL 1043

subtilisin-like protease; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2396434812  94 IAAPGVDILAAyTPANkdqgdSYEFLSGTSMACPHVSGIVALIKSLHPNWSPAAI----RSALVTTAS 157
Cdd:PTZ00262  534 LAAPGTNIYST-FPKN-----SYRKLNGTSMAAPHVAAIASLILSINPSLSYEEVirilKESIVQLPS 595

Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific proteases; Lantiobiotic (lanthionine-containing antibiotics) specific proteases are very similar in structure to serine proteases. Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides with antimicrobial activities against Gram-positive bacteria. The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP, nsuP, mutP, and nisP. EpiP, from Staphylococcus, is thought to cleave matured epidermin. NsuP, a dehydratase from Streptococcus and NisP, a membrane-anchored subtilisin-like serine protease from Lactococcus cleave nisin. MutP is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  74 LASFSSRGPSSItpevlkpDIAAPGVD--ILAAYTPAN--------KDQGDS------YEFLSGTSMACPHVSGIVALIK 137
Cdd:cd07482   203 LSSFSNYGNSRI-------DLAAPGGDflLLDQYGKEKwvnnglmtKEQILTtapeggYAYMYGTSLAAPKVSGALALII 275

                  ....*...
gi 2396434812 138 SLHPNWSP 145
Cdd:cd07482   276 DKNPLKKP 283

Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396434812  73 RLASFSSRGPSSITPEVLKPDIAA----------------PG--VDILAAYTPANKDQGDSYEFLSGTSMACPHVSGIVA 134
Cdd:cd07494   181 RASSYASGFRSKIYPGRQVPDVCGlvgmlphaaylmlpvpPGsqLDRSCAAFPDGTPPNDGWGVFSGTSAAAPQVAGVCA 260

                          90       100
                  ....*....|....*....|...
gi 2396434812 135 LIKSLHPNWSPAAIRSALVTTAS 157
Cdd:cd07494   261 LMLQANPGLSPERARSLLNKTAR 283

Peptidase S8 family domain, uncharacterized subfamily 2; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2396434812  91 KPDIAAPGVDIlaaYTPANKDqgdsyEFLSGTSMACPHVSGIVALIKSLHPN------WSPAAIRSALVTTA 156
Cdd:cd07488   184 KVLIVAPGSNY---NLPDGKD-----DFVSGTSFSAPLVTGIIALLLEFYDRqykkgnNNLIALRALVSSSV 247

Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase/subtilisin-like protease is produced by the symbiotic bacteria Prochloron spp. that inhabit didemnid family ascidians. The cyclic peptides of the patellamide class found in didemnid extracts are now known to be synthesized by the Prochloron spp. The prepatellamide is heterocyclized to form thiazole and oxazoline rings and the peptide is cleaved to form the two cyclic patellamides A and C. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution).

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2396434812  94 IAAPGVDILAAYTPANKDQgdsyefLSGTSMACPHVSGIVALIKSLH----PNWSPAAIRSALVTTA 156
Cdd:cd07476   189 ILAPGENILGAALGGEVVR------RSGTSFAAAIVAGIAALLLSLQlrrgAPPDPLAVRRALLETA 249